ID F4QQZ6_9CAUL Unreviewed; 312 AA.
AC F4QQZ6;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Signal peptidase I {ECO:0000256|ARBA:ARBA00019232, ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|ARBA:ARBA00013208, ECO:0000256|RuleBase:RU362042};
GN Name=lepB {ECO:0000313|EMBL:EGF90633.1};
GN ORFNames=ABI_36640 {ECO:0000313|EMBL:EGF90633.1};
OS Asticcacaulis biprosthecium C19.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Asticcacaulis.
OX NCBI_TaxID=715226 {ECO:0000313|EMBL:EGF90633.1, ECO:0000313|Proteomes:UP000006512};
RN [1] {ECO:0000313|Proteomes:UP000006512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C19 {ECO:0000313|Proteomes:UP000006512};
RA Brown P.J.B., Buechlein A., Hemmerich C., Brun Y.V.;
RT "Draft genome sequence of Brevundimonas diminuta.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of hydrophobic, N-terminal signal or leader sequences
CC from secreted and periplasmic proteins.; EC=3.4.21.89;
CC Evidence={ECO:0000256|ARBA:ARBA00000677,
CC ECO:0000256|RuleBase:RU362042};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU362042}; Single-
CC pass type II membrane protein {ECO:0000256|RuleBase:RU362042}.
CC -!- SIMILARITY: Belongs to the peptidase S26 family.
CC {ECO:0000256|ARBA:ARBA00009370, ECO:0000256|RuleBase:RU362042}.
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DR EMBL; GL883079; EGF90633.1; -; Genomic_DNA.
DR AlphaFoldDB; F4QQZ6; -.
DR STRING; 715226.ABI_36640; -.
DR MEROPS; S26.001; -.
DR eggNOG; COG0681; Bacteria.
DR HOGENOM; CLU_028723_1_2_5; -.
DR Proteomes; UP000006512; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR CDD; cd06530; S26_SPase_I; 1.
DR Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR InterPro; IPR019758; Pept_S26A_signal_pept_1_CS.
DR InterPro; IPR019757; Pept_S26A_signal_pept_1_Lys-AS.
DR InterPro; IPR019533; Peptidase_S26.
DR NCBIfam; TIGR02227; sigpep_I_bact; 1.
DR PANTHER; PTHR43390:SF1; CHLOROPLAST PROCESSING PEPTIDASE; 1.
DR PANTHER; PTHR43390; SIGNAL PEPTIDASE I; 1.
DR Pfam; PF10502; Peptidase_S26; 1.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
DR PROSITE; PS00760; SPASE_I_2; 1.
DR PROSITE; PS00761; SPASE_I_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042, ECO:0000313|EMBL:EGF90633.1};
KW Membrane {ECO:0000256|RuleBase:RU362042};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Transmembrane {ECO:0000256|RuleBase:RU362042};
KW Transmembrane helix {ECO:0000256|RuleBase:RU362042}.
FT TRANSMEM 74..93
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362042"
FT DOMAIN 72..284
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 102
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 163
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 312 AA; 34827 MW; ED4C3A2908253A4C CRC64;
MKDQGQILMN KDENTTPEPA DQPIVAAAAP AVDDAQPQVE LAKVQATKTE VEPEPAEAAP
RTAQEIAIAE IKEIGTVVGV AILLVLFLRT LFFQPFTIPS ASMEPNLYQG DYIIVSKWDY
GYSKHSIQFS PPLFNGRIFG RDPKRGDVVV FKLPVDNKTD YIKRVVGLPG DTVQLKNDQL
FINGQLVNTT TLGSIPGTAP GSGFRDETLT LQREELPDGR AHLMQDYVQD GPVDNTDIYT
VPEGHYFMMG DNRDNSQDSR YPMSVGGVDF VPAENLEGRA VLVLMSWKEG SSLWKPWTWL
NFHWDRFFKS LH
//
